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Poliovirus Virus-Like Particles (VLPs)

Creative Biolabs has been dedicated to providing first-class virus-like particle (VLP) products. We now have generated well-characterized poliovirus VLPs for our global customers. VLPs are multiprotein nanostructures or multiprotein formed from viral structural proteins but do not contain any nucleic acid genomes. Therefore, VLPs are not infective and ideal technology utilized for vaccines, antibody development, lipoparticle technology, delivery systems, bioimaging and cell targeting.

Poliovirus is a single-stranded, positive-sense RNA virus. It is a small virus (diameter about 27-30 nm) that lacks a viral envelope but has a capsid that surrounds its genome, which is approximately 7,500 nucleotides long. The capsid is consist of 60 copies of four structural proteins: VP1-VP4. The VP1, VP2, and VP3 contain antigen binding sites on their surface (also known as epitopes) to facilitate the antibody binding. The antibody recognition help to neutralize the virus either by inhibiting its replication or in other case making it a better target for phagocytosis or other forms of destruction. VP4, the fourth protein, is completely located inside the capsid and plays an unknown role in inducing antibodies. VP1 is the most exposed proteins of all the proteins on the surface and therefore plays an important role in the immune response. Besides that, as well as the other three viral proteins, VP1 are also involved in the virus binding to its receptor.

Poliovirus bound to a neuron receptor. Figure 1. Poliovirus bound to a neuron receptor.

Poliovirus infects host cells by binding to an immunoglobulin-like receptor CD155 on the cell surface. Interaction of poliovirus and CD155 facilitates an irreversible conformational change which is necessary for viral entry. Attached to the host cell membrane, the viral nucleic acid will be taken up by receptor-mediated endocytosis. On entry into the host cells, the virus hijacks the cell's translation machinery and inhibit cellular protein synthesis in favor of virus-specific protein production. Unlike the host cell's mRNAs, the 5' end of poliovirus RNA is extremely long and highly structured. This region contains over 700 nucleotides is called internal ribosome entry site (IRES), and it directs translation of the viral RNA.

Transmission electron microscope of Poliovirus VLPs Figure 2. Transmission electron microscope of Poliovirus VLPs.

Poliovirus VLPs can be typically used for:


Creative Biolabs offers risk-free VLPs construction service and high-quality products for your research needs. We now provide a wide range of ready-to-use VLP products (e.g. HBV VLP, HIV VLP, HPV VLP, CA16 VLP, EV71 VLP, polyomaviruses VLP, AAV VLP, bacteriophage Qβ VLP, Zika VLP) to satisfy every demand. With extensive experience, our scientists are confident in tailoring our customers the most cost-effective and fast-delivery service based on our well-established platforms. To ensure a smooth and successful completion of your project, an experienced scientist will be assigned to your project and work closely with you to keep you apprised of project progress while considering all your goals. Please feel free to inquire us for further discussions.

References

  1. Mendelsohn C L, Wimmer E, Racaniello V R. (1989). Cellular receptor for poliovirus: molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily. Cell, 56(5), 855-865.
  2. He Y, Mueller S, Chipman P R, et al. (2003). Complexes of poliovirus serotypes with their common cellular receptor, CD155. Journal of virology, 77(8), 4827-4835.
  3. Mueller S, Wimmer E, Cello J. (2005). Poliovirus and poliomyelitis: a tale of guts, brains, and an accidental event. Virus research, 111(2), 175-193.
  4. Harper D R. (2011). Viruses: Biology, applications, and control. Garland Science.



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